Abstract
Dispersed submicroscopic magnetic particles were used to probe viscoelasticity for cytoplasm and purified components of cytoplasm. An externally applied magnetic field exerted force on particles in cells, in filamentous actin (F-actin) solutions, or in F-actin gels formed by the addition of the actin gelation factor, actin-binding protein (ABP). The particle response to magnetic torque can be related to the viscoelastic properties of the fluids. We compared data obtained on F- actin by the magnetic particle method with data obtained on F-actin by means of a sliding plane viscoelastometer. F-actin solutions had a significant elasticity, which increased by 20-fold when gels were formed by ABP addition. Both methods gave consistent results, but the dispersed magnetic particles indicated quantitatively greater rigidity than the viscoelastometer (two and six times greater for F-actin solutions and for F-actin plus ABP gels, respectively). These differences may be due to the fact that, compared with traditional microrheometers, dispersed particle measurements are less affected by long-range heterogeneity or domain-like structure. The magnetometric method was used to examine the mechanical properties of cytoplasm within intact macrophages; the application of the same magnetometric technique to both cells and well-defined, purified protein systems is a first step toward interpreting the results obtained for living cells in molecular terms. The magnetic particle probe system is an effective nonoptical technique for determining the motile and mechanical properties of cells in vitro and in vivo.
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- Buxbaum R. E., Dennerll T., Weiss S., Heidemann S. R. F-actin and microtubule suspensions as indeterminate fluids. Science. 1987 Mar 20;235(4795):1511–1514. doi: 10.1126/science.2881354. [DOI] [PubMed] [Google Scholar]
- Cortese J. D., Frieden C. Microheterogeneity of actin gels formed under controlled linear shear. J Cell Biol. 1988 Oct;107(4):1477–1487. doi: 10.1083/jcb.107.4.1477. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Elson E. L. Cellular mechanics as an indicator of cytoskeletal structure and function. Annu Rev Biophys Biophys Chem. 1988;17:397–430. doi: 10.1146/annurev.bb.17.060188.002145. [DOI] [PubMed] [Google Scholar]
- Hartwig J. H., Shevlin P. The architecture of actin filaments and the ultrastructural location of actin-binding protein in the periphery of lung macrophages. J Cell Biol. 1986 Sep;103(3):1007–1020. doi: 10.1083/jcb.103.3.1007. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hartwig J. H., Stossel T. P. Structure of macrophage actin-binding protein molecules in solution and interacting with actin filaments. J Mol Biol. 1981 Jan 25;145(3):563–581. doi: 10.1016/0022-2836(81)90545-3. [DOI] [PubMed] [Google Scholar]
- Luby-Phelps K., Taylor D. L., Lanni F. Probing the structure of cytoplasm. J Cell Biol. 1986 Jun;102(6):2015–2022. doi: 10.1083/jcb.102.6.2015. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mastro A. M., Babich M. A., Taylor W. D., Keith A. D. Diffusion of a small molecule in the cytoplasm of mammalian cells. Proc Natl Acad Sci U S A. 1984 Jun;81(11):3414–3418. doi: 10.1073/pnas.81.11.3414. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nemoto I. A model of magnetization and relaxation of ferrimagnetic particles in the lung. IEEE Trans Biomed Eng. 1982 Dec;29(12):745–752. doi: 10.1109/TBME.1982.324869. [DOI] [PubMed] [Google Scholar]
- Nemoto I., Ogura K., Toyotama H. Estimation of the energy of cytoplasmic movements by magnetometry: effects of temperature and intracellular concentration of ATP. IEEE Trans Biomed Eng. 1989 Jun;36(6):598–607. doi: 10.1109/10.29454. [DOI] [PubMed] [Google Scholar]
- Newman J., Mroczka N., Schick K. L. Dynamic light scattering measurements of the diffusion of probes in filamentous actin solutions. Biopolymers. 1989 Feb;28(2):655–666. doi: 10.1002/bip.360280209. [DOI] [PubMed] [Google Scholar]
- Salmon E. D., Saxton W. M., Leslie R. J., Karow M. L., McIntosh J. R. Diffusion coefficient of fluorescein-labeled tubulin in the cytoplasm of embryonic cells of a sea urchin: video image analysis of fluorescence redistribution after photobleaching. J Cell Biol. 1984 Dec;99(6):2157–2164. doi: 10.1083/jcb.99.6.2157. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sato M., Leimbach G., Schwarz W. H., Pollard T. D. Mechanical properties of actin. J Biol Chem. 1985 Jul 15;260(14):8585–8592. [PubMed] [Google Scholar]
- Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
- Valberg P. A., Albertini D. F. Cytoplasmic motions, rheology, and structure probed by a novel magnetic particle method. J Cell Biol. 1985 Jul;101(1):130–140. doi: 10.1083/jcb.101.1.130. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Valberg P. A., Brain J. D. Generation and use of three types of iron-oxide aerosol. Am Rev Respir Dis. 1979 Nov;120(5):1013–1024. doi: 10.1164/arrd.1979.120.5.1013. [DOI] [PubMed] [Google Scholar]
- Valberg P. A., Butler J. P. Magnetic particle motions within living cells. Physical theory and techniques. Biophys J. 1987 Oct;52(4):537–550. doi: 10.1016/S0006-3495(87)83243-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Valberg P. A., Feldman H. A. Magnetic particle motions within living cells. Measurement of cytoplasmic viscosity and motile activity. Biophys J. 1987 Oct;52(4):551–561. doi: 10.1016/S0006-3495(87)83244-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zaner K. S., Hartwig J. H. The effect of filament shortening on the mechanical properties of gel-filtered actin. J Biol Chem. 1988 Apr 5;263(10):4532–4536. [PubMed] [Google Scholar]
- Zaner K. S., Stossel T. P. Physical basis of the rheologic properties of F-actin. J Biol Chem. 1983 Sep 25;258(18):11004–11009. [PubMed] [Google Scholar]
- Zaner K. S. The effect of the 540-kilodalton actin cross-linking protein, actin-binding protein, on the mechanical properties of F-actin. J Biol Chem. 1986 Jun 15;261(17):7615–7620. [PubMed] [Google Scholar]
